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P20594 (ANPRB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Atrial natriuretic peptide receptor 2

EC=4.6.1.2
Alternative name(s):
Atrial natriuretic peptide receptor type B
Short name=ANP-B
Short name=ANPR-B
Short name=NPR-B
Guanylate cyclase B
Short name=GC-B
Gene names
Name:NPR2
Synonyms:ANPRB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1047 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth. Ref.9 Ref.11

Catalytic activity

GTP = 3',5'-cyclic GMP + diphosphate.

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

Phosphorylation of the protein kinase-like domain is required for full activation by CNP By similarity.

Involvement in disease

Acromesomelic dysplasia, Maroteaux type (AMDM) [MIM:602875]: An autosomal recessive acromesomelic chondrodysplasia. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMDM is characterized by axial skeletal involvement with wedging of vertebral bodies. In AMDM all skeletal elements are present but show abnormal rates of linear growth.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Sequence similarities

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.

Contains 1 guanylate cyclase domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processcGMP biosynthesis
Osteogenesis
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Dwarfism
   DomainSignal
Transmembrane
Transmembrane helix
   LigandGTP-binding
Nucleotide-binding
   Molecular functionLyase
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone development

Inferred from electronic annotation. Source: Ensembl

cGMP biosynthetic process

Inferred from direct assay Ref.9. Source: UniProtKB

cell surface receptor signaling pathway

Traceable author statement PubMed 1327579. Source: ProtInc

cellular response to granulocyte macrophage colony-stimulating factor stimulus

Inferred from expression pattern PubMed 14687666. Source: UniProtKB

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

ossification

Inferred from electronic annotation. Source: UniProtKB-KW

receptor guanylyl cyclase signaling pathway

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of blood pressure

Traceable author statement Ref.2. Source: ProtInc

signal transduction

Non-traceable author statement Ref.2. Source: ProtInc

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement PubMed 1327579. Source: ProtInc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: Ensembl

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

guanylate cyclase activity

Inferred from direct assay Ref.9. Source: UniProtKB

hormone binding

Inferred from physical interaction Ref.8Ref.9. Source: UniProtKB

natriuretic peptide receptor activity

Inferred from direct assay Ref.8Ref.9. Source: UniProtKB

peptide hormone binding

Inferred from electronic annotation. Source: Ensembl

protein kinase activity

Inferred from electronic annotation. Source: InterPro

receptor activity

Traceable author statement Ref.2. Source: ProtInc

transmembrane signaling receptor activity

Traceable author statement PubMed 1327579. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P20594-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: P20594-2)

Also known as: NPR-BI;

The sequence of this isoform differs from the canonical sequence as follows:
     964-1047: PVCAGVVGLK...GERKGPPGLL → KADSHSSPSLHLSQTLPTCFFSKGQSVLGLLA
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 10471025Atrial natriuretic peptide receptor 2
PRO_0000012364

Regions

Topological domain23 – 458436Extracellular Potential
Transmembrane459 – 47820Helical; Potential
Topological domain479 – 1047569Cytoplasmic Potential
Domain513 – 786274Protein kinase
Domain861 – 991131Guanylate cyclase

Amino acid modifications

Modified residue5131Phosphoserine Ref.12
Modified residue5161Phosphothreonine Ref.12
Modified residue5181Phosphoserine Ref.12
Modified residue5231Phosphoserine Ref.12
Modified residue5261Phosphoserine Ref.12
Modified residue5291Phosphothreonine Ref.12
Glycosylation241N-linked (GlcNAc...) Potential
Glycosylation351N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation1951N-linked (GlcNAc...) Potential
Glycosylation2441N-linked (GlcNAc...) Potential
Glycosylation2771N-linked (GlcNAc...) Potential
Glycosylation3491N-linked (GlcNAc...) Potential
Disulfide bond75 ↔ 101 By similarity
Disulfide bond439Interchain Probable
Disulfide bond448Interchain Probable

Natural variations

Alternative sequence964 – 104784PVCAG…PPGLL → KADSHSSPSLHLSQTLPTCF FSKGQSVLGLLA in isoform Short.
VSP_001810
Natural variant321P → T in AMDM. Ref.11
Corresponds to variant rs28931581 [ dbSNP | Ensembl ].
VAR_022583
Natural variant1151W → G in AMDM; markedly deficient activity. Ref.11
Corresponds to variant rs28931582 [ dbSNP | Ensembl ].
VAR_022584
Natural variant1761D → E in AMDM. Ref.11
Corresponds to variant rs28929479 [ dbSNP | Ensembl ].
VAR_022585
Natural variant2321M → I. Ref.13
Corresponds to variant rs55747238 [ dbSNP | Ensembl ].
VAR_042219
Natural variant2971T → M in AMDM; markedly deficient activity. Ref.11
VAR_022586
Natural variant3381Y → C in AMDM. Ref.11
VAR_022587
Natural variant4091A → T in AMDM. Ref.11
VAR_022588
Natural variant4131G → E in AMDM; markedly deficient activity. Ref.11
VAR_022589
Natural variant7081Y → C in AMDM. Ref.11
VAR_022590
Natural variant7711Q → E.
Corresponds to variant rs5816 [ dbSNP | Ensembl ].
VAR_011968
Natural variant7761R → W in AMDM. Ref.11
VAR_022591
Natural variant8821V → I. Ref.13
Corresponds to variant rs55700371 [ dbSNP | Ensembl ].
VAR_042220
Natural variant9571R → C in AMDM. Ref.11
VAR_022592
Natural variant9591G → A in AMDM. Ref.11
VAR_022593

Experimental info

Sequence conflict7551T → S in BAA81737. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 817FB74D6B31F7EF

FASTA1,047117,022
        10         20         30         40         50         60 
MALPSLLLLV AALAGGVRPP GARNLTLAVV LPEHNLSYAW AWPRVGPAVA LAVEALGRAL 

        70         80         90        100        110        120 
PVDLRFVSSE LEGACSEYLA PLSAVDLKLY HDPDLLLGPG CVYPAASVAR FASHWRLPLL 

       130        140        150        160        170        180 
TAGAVASGFS AKNDHYRTLV RTGPSAPKLG EFVVTLHGHF NWTARAALLY LDARTDDRPH 

       190        200        210        220        230        240 
YFTIEGVFEA LQGSNLSVQH QVYAREPGGP EQATHFIRAN GRIVYICGPL EMLHEILLQA 

       250        260        270        280        290        300 
QRENLTNGDY VFFYLDVFGE SLRAGPTRAT GRPWQDNRTR EQAQALREAF QTVLVITYRE 

       310        320        330        340        350        360 
PPNPEYQEFQ NRLLIRARED FGVELGPSLM NLIAGCFYDG ILLYAEVLNE TIQEGGTRED 

       370        380        390        400        410        420 
GLRIVEKMQG RRYHGVTGLV VMDKNNDRET DFVLWAMGDL DSGDFQPAAH YSGAEKQIWW 

       430        440        450        460        470        480 
TGRPIPWVKG APPSDNPPCA FDLDDPSCDK TPLSTLAIVA LGTGITFIMF GVSSFLIFRK 

       490        500        510        520        530        540 
LMLEKELASM LWRIRWEELQ FGNSERYHKG AGSRLTLSLR GSSYGSLMTA HGKYQIFANT 

       550        560        570        580        590        600 
GHFKGNVVAI KHVNKKRIEL TRQVLFELKH MRDVQFNHLT RFIGACIDPP NICIVTEYCP 

       610        620        630        640        650        660 
RGSLQDILEN DSINLDWMFR YSLINDLVKG MAFLHNSIIS SHGSLKSSNC VVDSRFVLKI 

       670        680        690        700        710        720 
TDYGLASFRS TAEPDDSHAL YAKKLWTAPE LLSGNPLPTT GMQKADVYSF GIILQEIALR 

       730        740        750        760        770        780 
SGPFYLEGLD LSPKEIVQKV RNGQRPYFRP SIDRTQLNEE LVLLMERCWA QDPAERPDFG 

       790        800        810        820        830        840 
QIKGFIRRFN KEGGTSILDN LLLRMEQYAN NLEKLVEERT QAYLEEKRKA EALLYQILPH 

       850        860        870        880        890        900 
SVAEQLKRGE TVQAEAFDSV TIYFSDIVGF TALSAESTPM QVVTLLNDLY TCFDAIIDNF 

       910        920        930        940        950        960 
DVYKVETIGD AYMVVSGLPG RNGQRHAPEI ARMALALLDA VSSFRIRHRP HDQLRLRIGV 

       970        980        990       1000       1010       1020 
HTGPVCAGVV GLKMPRYCLF GDTVNTASRM ESNGQALKIH VSSTTKDALD ELGCFQLELR 

      1030       1040 
GDVEMKGKGK MRTYWLLGER KGPPGLL 

« Hide

Isoform Short (NPR-BI) [UniParc].

Checksum: 745D41E451E0D7DF
Show »

FASTA995111,208

References

« Hide 'large scale' references
[1]"Differential activation by atrial and brain natriuretic peptides of two different receptor guanylate cyclases."
Chang M.S., Lowe D.G., Lewis M., Hellmiss R., Chen E., Goeddel D.V.
Nature 341:68-72(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM LONG).
Tissue: Brain.
[2]"Structure of the type B human natriuretic peptide receptor gene and association of a novel microsatellite polymorphism with essential hypertension."
Rehemudula D., Nakayama T., Soma M., Takahashi Y., Uwabo J., Sato M., Izumi Y., Kanmatsuse K., Ozawa Y.
Circ. Res. 84:605-610(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[3]"cGMP-dependent and -independent inhibition of a K+ conductance by natriuretic peptides: molecular and functional studies in human proximal tubule cells."
Hirsch J.R., Meyer M., Maegert H.-J., Forssmann W.-G., Mollerup S., Herter P., Weber G., Cermak R., Ankorina-Stark I., Schlatter E., Kruhoffer M.
J. Am. Soc. Nephrol. 10:472-480(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Tissue: Kidney.
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
Tissue: Brain.
[8]"Extracellular domain-IgG fusion proteins for three human natriuretic peptide receptors. Hormone pharmacology and application to solid phase screening of synthetic peptide antisera."
Bennett B.D., Bennett G.L., Vitangcol R.V., Jewett J.R., Burnier J., Henzel W., Lowe D.G.
J. Biol. Chem. 266:23060-23067(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: LIGAND-BINDING.
[9]"Selective activation of the B natriuretic peptide receptor by C-type natriuretic peptide (CNP)."
Koller K.J., Lowe D.G., Bennett G.L., Minamino N., Kangawa K., Matsuo H., Goeddel D.V.
Science 252:120-123(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[11]"Mutations in the transmembrane natriuretic peptide receptor NPR-B impair skeletal growth and cause acromesomelic dysplasia, type Maroteaux."
Bartels C.F., Buekuelmez H., Padayatti P., Rhee D.K., van Ravenswaaij-Arts C., Pauli R.M., Mundlos S., Chitayat D., Shih L.-Y., Al-Gazali L.I., Kant S., Cole T., Morton J., Cormier-Daire V., Faivre L., Lees M., Kirk J., Mortier G.R. expand/collapse author list , Leroy J., Zabel B., Kim C.A., Crow Y., Braverman N.E., van den Akker F., Warman M.L.
Am. J. Hum. Genet. 75:27-34(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, VARIANTS AMDM THR-32; GLY-115; GLU-176; MET-297; CYS-338; THR-409; GLU-413; CYS-708; TRP-776; CYS-957 AND ALA-959, CHARACTERIZATION OF VARIANTS AMDM GLY-115; MET-297 AND GLU-413.
[12]"Mass spectrometric identification of phosphorylation sites in guanylyl cyclase A and B."
Yoder A.R., Stone M.D., Griffin T.J., Potter L.R.
Biochemistry 49:10137-10145(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-513; THR-516; SER-518; SER-523; SER-526 AND THR-529.
[13]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-232 AND ILE-882.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB005647 Genomic DNA. Translation: BAA81737.1.
AJ005282 mRNA. Translation: CAA06466.1.
AL133410 Genomic DNA. Translation: CAI10987.1.
EU326311 Genomic DNA. Translation: ACA05920.1.
EU326311 Genomic DNA. Translation: ACA05921.1.
CH471071 Genomic DNA. Translation: EAW58338.1.
CH471071 Genomic DNA. Translation: EAW58337.1.
CH471071 Genomic DNA. Translation: EAW58339.1.
CH471071 Genomic DNA. Translation: EAW58340.1.
BC023017 mRNA. Translation: AAH23017.1.
PIROYHUBR. S05514.
RefSeqNP_003986.2. NM_003995.3.
UniGeneHs.78518.

3D structure databases

ProteinModelPortalP20594.
SMRP20594. Positions 24-442, 503-831, 854-1036.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110942. 4 interactions.
IntActP20594. 1 interaction.
STRING9606.ENSP00000341083.

Chemistry

BindingDBP20594.
ChEMBLCHEMBL2111337.
DrugBankDB01613. Erythrityl Tetranitrate.
DB04899. Nesiritide.
GuidetoPHARMACOLOGY1748.

PTM databases

PhosphoSiteP20594.

Polymorphism databases

DMDM113916.

Proteomic databases

PaxDbP20594.
PRIDEP20594.

Protocols and materials databases

DNASU4882.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342694; ENSP00000341083; ENSG00000159899. [P20594-1]
GeneID4882.
KEGGhsa:4882.
UCSCuc003zyd.3. human. [P20594-1]

Organism-specific databases

CTD4882.
GeneCardsGC09P035792.
H-InvDBHIX0034787.
HGNCHGNC:7944. NPR2.
HPAHPA011977.
MIM108961. gene.
602875. phenotype.
neXtProtNX_P20594.
Orphanet40. Acromesomelic dysplasia, Maroteaux type.
329191. Tall stature - scoliosis - macrodactyly of the great toes.
PharmGKBPA257.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG051862.
InParanoidP20594.
KOK12324.
OMAAAKSEHY.
OrthoDBEOG7Z69BJ.
PhylomeDBP20594.
TreeFamTF106338.

Gene expression databases

ArrayExpressP20594.
BgeeP20594.
CleanExHS_NPR2.
GenevestigatorP20594.

Family and domain databases

Gene3D3.30.70.1230. 1 hit.
InterProIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011009. Kinase-like_dom.
IPR001170. Ntpep_rcpt.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00255. NATPEPTIDER.
SMARTSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00458. ANF_RECEPTORS. 1 hit.
PS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNPR2. human.
GeneWikiNPR2.
GenomeRNAi4882.
NextBio18792.
PROP20594.
SOURCESearch...

Entry information

Entry nameANPRB_HUMAN
AccessionPrimary (citable) accession number: P20594
Secondary accession number(s): B0ZBF2 expand/collapse secondary AC list , B0ZBF3, D3DRP3, D3DRP4, O60871, Q4VAK7, Q5TCV2, Q8TA93, Q9UQ50
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM